C81Q1_SESIN
ID C81Q1_SESIN Reviewed; 506 AA.
AC Q33DY0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=(+)-piperitol/(+)-sesamin synthase CYP81Q1 {ECO:0000305};
DE EC=1.14.19.74 {ECO:0000269|PubMed:16785429};
DE AltName: Full=Cytochrome P450 81Q1 {ECO:0000303|PubMed:16785429};
DE AltName: Full=Piperitol synthase CYP81Q1 {ECO:0000305};
DE AltName: Full=Sesamin synthase CYP81Q1 {ECO:0000305};
GN Name=CYP81Q1 {ECO:0000303|PubMed:16785429};
OS Sesamum indicum (Oriental sesame) (Sesamum orientale).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX NCBI_TaxID=4182;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16785429; DOI=10.1073/pnas.0603865103;
RA Ono E., Nakai M., Fukui Y., Tomimori N., Fukuchi-Mizutani M., Saito M.,
RA Satake H., Tanaka T., Katsuta M., Umezawa T., Tanaka Y.;
RT "Formation of two methylenedioxy bridges by a Sesamum CYP81Q protein
RT yielding a furofuran lignan, (+)-sesamin.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10116-10121(2006).
CC -!- FUNCTION: Involved in the biosynthesis of (+)-sesamin, a furofuran
CC class lignan (PubMed:16785429). Functions in a dual catalytic mode
CC (PubMed:16785429). Catalyzes the synthesis of (+)-sesamin from
CC (+)- pinoresinol by formation of two successive methylenedioxy bridges
CC on (+)-pinoresinol and (+)-piperitol, respectively (PubMed:16785429).
CC {ECO:0000269|PubMed:16785429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-piperitol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (+)-sesamin + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56780, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:66470,
CC ChEBI:CHEBI:141003; EC=1.14.19.74;
CC Evidence={ECO:0000269|PubMed:16785429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56781;
CC Evidence={ECO:0000269|PubMed:16785429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-pinoresinol + O2 + reduced [NADPH--hemoprotein reductase]
CC = (+)-piperitol + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:56776, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:40, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:141003; EC=1.14.19.74;
CC Evidence={ECO:0000269|PubMed:16785429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56777;
CC Evidence={ECO:0000269|PubMed:16785429};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 uM for (+)-pinoresinol {ECO:0000269|PubMed:16785429};
CC KM=11.7 uM for (+)-piperitol {ECO:0000269|PubMed:16785429};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16785429}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds and leaves.
CC {ECO:0000269|PubMed:16785429}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB194714; BAE48234.1; -; mRNA.
DR RefSeq; NP_001306620.1; NM_001319691.1.
DR SMR; Q33DY0; -.
DR EnsemblPlants; SIN_1025734.t; SIN_1025734.t; SIN_1025734.
DR GeneID; 105177765; -.
DR Gramene; SIN_1025734.t; SIN_1025734.t; SIN_1025734.
DR KEGG; sind:105177765; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q33DY0; -.
DR BRENDA; 1.14.19.74; 5697.
DR Proteomes; UP000504604; Linkage group LG15.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="(+)-piperitol/(+)-sesamin synthase CYP81Q1"
FT /id="PRO_0000455167"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 439
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
SQ SEQUENCE 506 AA; 57246 MW; A818182A92C877F4 CRC64;
MEAEMLYSAL ALTFAIFMVY RILSNSQDKR SLTKLPPSPP GWLPVIGHAH LMKNLLHRTL
YDFSQKLGPI FSIRFGSRLV VVVSSSSLVE ECFTKYDIVL ANRPQASVDR RSLGFSTTSV
IGAPYGDHWR NLRKLCDLEV FAPTRLASFL SIRLDERDRM ISALYKISSA GFAKVNLEAK
IVELTFNNIM RMVAAKRYYG EEAEDDEEAK RFRDLTKEAL ELTSASNPGE IFPILRWLGC
NGLEKKLAVH SRKTDEFMQG LLDEHRRGER QNTMVDHLLS LQESQPEYYT DEIITGLIVA
LIIAGTDASV VTTEWAMSLL LNHPKVLEKA RKELDTLVGH ERMVDEHDLP KLRYLHCIVL
ETLRLFPSVP TLVPHEPSED CKIGGYNVPK GTMVLVNAWA IHRDPKVWDD PLSFKPDRFE
IMEVETHKLL PFGMGRRACP GAGLAQKFVG LALGSLIQCF DWERTSPEKI DLNEGSGITL
PKAKTLEAMC KPRHVMEKVL RQVSNV
